P11497 (ACACA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA carboxylase 1
Short name=ACC1
EC=6.4.1.2

Alternative name(s):
ACC-alpha

Including the following 1 domains:

1. Biotin carboxylase
   EC=6.3.4.14

Gene names

Name:	Acaca
Synonyms:	Acac

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	2345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
Cofactor	Biotin. Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization By similarity. Activity is increased by phosphorylation.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity By similarity.
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked. Phosphorylation on Ser-1262 is required for interaction with BRCA1 By similarity. Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear. Ref.5 Ref.6 Ref.9 Ref.10
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from direct assay PubMed 12949377. Source: RGD fatty acid biosynthetic process Inferred from direct assay PubMed 11735100. Source: RGD malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from expression pattern PubMed 16979414. Source: RGD response to organic cyclic compound Inferred from mutant phenotype PubMed 12842871. Source: RGD
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay PubMed 12949377. Source: RGD acetyl-CoA carboxylase activity Inferred from direct assay PubMed 11735100PubMed 12949377. Source: RGD biotin binding Inferred from mutant phenotype PubMed 12949377. Source: RGD biotin carboxylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11497-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P11497-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1189-1196: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2345	2345	Acetyl-CoA carboxylase 1		PRO_0000146765
Regions
	Domain	116 – 617	502	Biotin carboxylation
	Domain	274 – 465	192	ATP-grasp
	Domain	751 – 817	67	Biotinyl-binding
	Domain	1697 – 2193	497	Carboxyltransferase
	Nucleotide binding	314 – 319	6	ATP Potential
Sites
	Active site	440	1	By similarity
	Metal binding	423	1	Manganese 1 By similarity
	Metal binding	436	1	Manganese 1 By similarity
	Metal binding	436	1	Manganese 2 By similarity
	Metal binding	438	1	Manganese 2 By similarity
	Binding site	1822	1	Coenzyme A By similarity
	Binding site	2126	1	Coenzyme A By similarity
	Binding site	2128	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	5	1	Phosphoserine By similarity
	Modified residue	23	1	Phosphoserine By similarity
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	29	1	Phosphoserine By similarity
	Modified residue	47	1	Phosphoserine By similarity
	Modified residue	52	1	Phosphoserine By similarity
	Modified residue	77	1	Phosphoserine
	Modified residue	79	1	Phosphoserine; by AMPK Ref.9 Ref.11
	Modified residue	785	1	N6-biotinyllysine
	Modified residue	1200	1	Phosphoserine; by AMPK; in vitro Ref.6 Ref.9
	Modified residue	1215	1	Phosphoserine; by AMPK; in vitro Ref.9
	Modified residue	1262	1	Phosphoserine By similarity
	Modified residue	1333	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1189 – 1196	8	Missing in isoform 2.		VSP_011753

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 78E9CF9ADE1E8771	FASTA	2,345	265,194
	10 20 30 40 50 60 MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD 70 80 90 100 110 120 LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV 130 140 150 160 170 180 LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG 190 200 210 220 230 240 ANNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG 250 260 270 280 290 300 DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 310 320 330 340 350 360 EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ 370 380 390 400 410 420 ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG 430 440 450 460 470 480 TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG 490 500 510 520 530 540 VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF 550 560 570 580 590 600 SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 610 620 630 640 650 660 SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF LHSLERGQVL 670 680 690 700 710 720 PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS 730 740 750 760 770 780 SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE 790 800 810 820 830 840 IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS 850 860 870 880 890 900 TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD 910 920 930 940 950 960 IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF 970 980 990 1000 1010 1020 FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM 1030 1040 1050 1060 1070 1080 NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA 1090 1100 1110 1120 1130 1140 RQVLIASHLP SYDVRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS 1150 1160 1170 1180 1190 1200 NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1210 1220 1230 1240 1250 1260 FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE VMGCFCDSPP 1270 1280 1290 1300 1310 1320 QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE 1330 1340 1350 1360 1370 1380 HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL 1390 1400 1410 1420 1430 1440 ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY 1450 1460 1470 1480 1490 1500 LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1510 1520 1530 1540 1550 1560 RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY 1570 1580 1590 1600 1610 1620 GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF 1630 1640 1650 1660 1670 1680 LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG 1690 1700 1710 1720 1730 1740 NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS 1750 1760 1770 1780 1790 1800 EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1810 1820 1830 1840 1850 1860 MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE 1870 1880 1890 1900 1910 1920 VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY MPKNVHSSVP LLNSKDPIDR 1930 1940 1950 1960 1970 1980 IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI 1990 2000 2010 2020 2030 2040 PVGVVAVETR TVELSVPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM 2050 2060 2070 2080 2090 2100 VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2110 2120 2130 2140 2150 2160 PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER 2170 2180 2190 2200 2210 2220 KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR 2230 2240 2250 2260 2270 2280 LLLEDLVKKK IHSANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE 2290 2300 2310 2320 2330 2340 DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST
	Isoform 2 [UniParc]. Checksum: 9590EEFFE39D73CD	FASTA	2,337	264,328
	10 20 30 40 50 60 MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD 70 80 90 100 110 120 LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV 130 140 150 160 170 180 LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG 190 200 210 220 230 240 ANNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG 250 260 270 280 290 300 DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 310 320 330 340 350 360 EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ 370 380 390 400 410 420 ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG 430 440 450 460 470 480 TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG 490 500 510 520 530 540 VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF 550 560 570 580 590 600 SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 610 620 630 640 650 660 SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF LHSLERGQVL 670 680 690 700 710 720 PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS 730 740 750 760 770 780 SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE 790 800 810 820 830 840 IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS 850 860 870 880 890 900 TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD 910 920 930 940 950 960 IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF 970 980 990 1000 1010 1020 FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM 1030 1040 1050 1060 1070 1080 NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA 1090 1100 1110 1120 1130 1140 RQVLIASHLP SYDVRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS 1150 1160 1170 1180 1190 1200 NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR MSFASNLNHY 1210 1220 1230 1240 1250 1260 GMTHVASVSD VLLDNAFTPP CQRMGGMVSF RTFEDFVRIF DEVMGCFCDS PPQSPTFPES 1270 1280 1290 1300 1310 1320 GHTSLYDEDK VPRDEPIHIL NVAIKTDGDI EDDRLAAMFR EFTQQNKATL VEHGIRRLTF 1330 1340 1350 1360 1370 1380 LVAQKDFRKQ VNCEVDQRFH REFPKFFTFR ARDKFEEDRI YRHLEPALAF QLELNRMRNF 1390 1400 1410 1420 1430 1440 DLTAIPCANH KMHLYLGAAK VEVGTEVTDY RFFVRAIIRH SDLVTKEASF EYLQNEGERL 1450 1460 1470 1480 1490 1500 LLEAMDELEV AFNNTNVRTD CNHIFLNFVP TVIMDPSKIE ESVRSMVMRY GSRLWKLRVL 1510 1520 1530 1540 1550 1560 QAELKINIRL TTTGKAIPIR LFLTNESGYY LDISLYKEVT DSRTAQIMFQ AYGDKQGPLH 1570 1580 1590 1600 1610 1620 GMLINTPYVT KDLLQSKRFQ AQSLGTTYIY DIPEMFRQSL IKLWESMSTQ AFLPSPPLPS 1630 1640 1650 1660 1670 1680 DILTYTELVL DDQGQLVHMN RLPGGNEIGM VAWKMSLKSP EYPDGRDVIV IGNDITYRIG 1690 1700 1710 1720 1730 1740 SFGPQEDLLF LRASELARAE GIPRIYVAAN SGARIGLAEE IRHMFHVAWV DSEDPYKGYK 1750 1760 1770 1780 1790 1800 YLYLTPQDYK RVSALNSVHC EHVEDEGESR YKITDIIGKE EGLGAENLRG SGMIAGESSL 1810 1820 1830 1840 1850 1860 AYDEIITISL VTCRAIGIGA YLVRLGQRTI QVENSHLILT GAGALNKVLG REVYTSNNQL 1870 1880 1890 1900 1910 1920 GGIQIMHNNG VTHCTVCDDF EGVFTVLHWL SYMPKNVHSS VPLLNSKDPI DRIIEFVPTK 1930 1940 1950 1960 1970 1980 APYDPRWMLA GRPHPTQKGQ WLSGFFDYGS FSEIMQPWAQ TVVVGRARLG GIPVGVVAVE 1990 2000 2010 2020 2030 2040 TRTVELSVPA DPANLDSEAK IIQQAGQVWF PDSAFKTYQA IKDFNREGLP LMVFANWRGF 2050 2060 2070 2080 2090 2100 SGGMKDMYDQ VLKFGAYIVD GLRECSQPVM VYIPPQAELR GGSWVVIDPT INPRHMEMYA 2110 2120 2130 2140 2150 2160 DRESRGSVLE PEGTVEIKFR KKDLVKTMRR VDPVYIRLAE RLGTPELSPT ERKELESKLK 2170 2180 2190 2200 2210 2220 EREEFLIPIY HQVAVQFADL HDTPGRMQEK GVINDILDWK TSRTFFYWRL RRLLLEDLVK 2230 2240 2250 2260 2270 2280 KKIHSANPEL TDGQIQAMLR RWFVEVEGTV KAYVWDNNKD LVEWLEKQLT EEDGVRSVIE 2290 2300 2310 2320 2330 ENIKYISRDY VLKQIRSLVQ ANPEVAMDSI VHMTQHISPT QRAEVVRILS TMDSPST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the coding sequence and primary amino acid sequence of acetyl-coenzyme A carboxylase." Lopez-Casillas F., Bai D.-H., Luo X., Kong I.-S., Hermodson M.A., Kim K.-H. Proc. Natl. Acad. Sci. U.S.A. 85:5784-5788(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Structural features of the acetyl-CoA carboxylase gene: mechanisms for the generation of mRNAs with 5' end heterogeneity." Luo X.N., Park K., Lopez-Casillas F., Kim K.-H. Proc. Natl. Acad. Sci. U.S.A. 86:4042-4046(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Fine-mapping and comprehensive transcript analysis reveals nonsynonymous variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome 10." Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P., Radecki T., Joe B. Genomics 89:343-353(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Dahl salt-sensitive and Lewis.
[4]	"Heterogeneity at the 5' end of rat acetyl-coenzyme A carboxylase mRNA. Lipogenic conditions enhance synthesis of a unique mRNA in liver." Lopez-Casillas F., Kim K.-H. J. Biol. Chem. 264:7176-7184(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
[5]	"Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase." Munday M.R., Campbell D.G., Carling D., Hardie D.G. Eur. J. Biochem. 175:331-338(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-85 AND 1198-1201, PHOSPHORYLATION.
[6]	"Acetyl-CoA carboxylase mRNA species with or without inhibitory coding sequence for Ser-1200 phosphorylation." Kong I.-S., Lopez-Casillas F., Kim K.-H. J. Biol. Chem. 265:13695-13701(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), PHOSPHORYLATION AT SER-1200.
[7]	"Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase." Winz R., Hess D., Aebersold R., Brownsey R.W. J. Biol. Chem. 269:14438-14445(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Strain: Wistar. Tissue: Liver.
[8]	"Analysis of the biotin-binding site on acetyl-CoA carboxylase from rat." Bai D.-H., Moon T.-W., Lopez-Casillas F., Andrews P.C., Kim K.-H. Eur. J. Biochem. 182:239-245(1989) [PubMed] [Europe PMC] [Abstract] Cited for: BIOTIN-BINDING SITE.
[9]	"Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets." Davies S.P., Carling D., Munday M.R., Hardie D.G. Eur. J. Biochem. 203:615-623(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.
[10]	"Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A." Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A., Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B. J. Appl. Physiol. 82:219-225(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY AMPK.
[11]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03808 mRNA. Translation: AAA40653.1. M26731 Genomic DNA. Translation: AAA40652.1. EF121986 mRNA. Translation: ABL63425.1. EF121987 mRNA. Translation: ABL63426.1. M26195 mRNA. Translation: AAA40654.1. M26196 mRNA. Translation: AAA40655.1. M26197 mRNA. Translation: AAA40656.1. M55315 mRNA. No translation available.
IPI	IPI00194102. IPI00567332.
PIR	A35578.
RefSeq	NP_071529.1. NM_022193.1.
UniGene	Rn.163753. Rn.217177. Rn.44372.
3D structure databases
ProteinModelPortal	P11497.
SMR	P11497. Positions 96-615, 741-833, 1791-2118.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000050703.
PTM databases
PhosphoSite	P11497.
Proteomic databases
PaxDb	P11497.
PRIDE	P11497.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	60581.
KEGG	rno:60581.
Organism-specific databases
CTD	31.
RGD	621248. Acaca.
Phylogenomic databases
eggNOG	COG0511.
HOGENOM	HOG000214115.
HOVERGEN	HBG005371.
InParanoid	P11497.
KO	K11262.
OrthoDB	EOG4X0MRD.
Enzyme and pathway databases
BRENDA	6.4.1.2. 5301.
UniPathway	UPA00655; UER00711.
Gene expression databases
ArrayExpress	P11497.
Genevestigator	P11497.
GermOnline	ENSRNOG00000034013. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
InterPro	IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005481. CarbamoylP_synth_lsu_N. IPR000022. Carboxyl_trans. IPR005479. CbamoylP_synth_lsu-like_ATP-bd. IPR011763. COA_CT_C. IPR011762. COA_CT_N. IPR016185. PreATP-grasp_dom. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF08326. ACC_central. 1 hit. PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF01039. Carboxyl_trans. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS50989. COA_CT_CTER. 1 hit. PS50980. COA_CT_NTER. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P11497.
ChEMBL	CHEMBL2397.
NextBio	612298.

Entry information

Entry name

ACACA_RAT

Accession

Primary (citable) accession number: P11497
Secondary accession number(s): A1EC79, P97902

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program